STRINGSTRING
STRING protein interaction network
Nodes:
Network nodes represent proteins
splice isoforms or post-translational modifications are collapsed, i.e. each node represents all the proteins produced by a single, protein-coding gene locus.
Node Color
colored nodes:
query proteins and first shell of interactors
white nodes:
second shell of interactors
Node Content
empty nodes:
proteins of unknown 3D structure
filled nodes:
a 3D structure is known or predicted
Edges:
Edges represent protein-protein associations
associations are meant to be specific and meaningful, i.e. proteins jointly contribute to a shared function; this does not necessarily mean they are physically binding to each other.
Known Interactions
from curated databases
experimentally determined
Predicted Interactions
gene neighborhood
gene fusions
gene co-occurrence
Others
textmining
co-expression
protein homology
Your Input:
Neighborhood
Gene Fusion
Cooccurrence
Coexpression
Experiments
Databases
Textmining
[Homology]
Score
ppaInorganic pyrophosphatase; Catalyzes the hydrolysis of inorganic pyrophosphate (PPi) forming two phosphate ions. (176 aa)    
Predicted Functional Partners:
atpF
F0F1 ATP synthase subunit B; Component of the F(0) channel, it forms part of the peripheral stalk, linking F(1) to F(0); Belongs to the ATPase B chain family.
   
 
 0.954
atpH
F0F1 ATP synthase subunit delta; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
   
 
 0.949
atpE
ATP F0F1 synthase subunit C; F(1)F(0) ATP synthase produces ATP from ADP in the presence of a proton or sodium gradient. F-type ATPases consist of two structural domains, F(1) containing the extramembraneous catalytic core and F(0) containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F(1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation.
   
 
 0.946
atpA_2
F0F1 ATP synthase subunit alpha; Derived by automated computational analysis using gene prediction method: Protein Homology.
   
 
 0.941
atpG
F0F1 ATP synthase subunit gamma; Produces ATP from ADP in the presence of a proton gradient across the membrane. The gamma chain is believed to be important in regulating ATPase activity and the flow of protons through the CF(0) complex.
   
 
 0.939
ppk_2
RNA degradosome polyphosphate kinase; Derived by automated computational analysis using gene prediction method: Protein Homology.
     
 0.928
atpD
F0F1 ATP synthase subunit beta; Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits.
   
 
 0.928
atpB
F0F1 ATP synthase subunit A; Key component of the proton channel; it plays a direct role in the translocation of protons across the membrane. Belongs to the ATPase A chain family.
   
 
 0.920
atpC
F0F1 ATP synthase subunit epsilon; Produces ATP from ADP in the presence of a proton gradient across the membrane.
   
 
  0.913
efp
Elongation factor P; Involved in peptide bond synthesis. Alleviates ribosome stalling that occurs when 3 or more consecutive Pro residues or the sequence PPG is present in a protein, possibly by augmenting the peptidyl transferase activity of the ribosome. Modification of Lys-34 is required for alleviation; Belongs to the elongation factor P family.
   
  
 0.798
Your Current Organism:
Pantoea agglomerans
NCBI taxonomy Id: 549
Other names: ATCC 27155, Bacillus milletiae, Bacterium herbicola, CCUG 539, CFBP 3845, CIP 57.51, DSM 3493, Enterobacter agglomerans, Erwinia herbicola, Erwinia milletiae, ICMP 12534, ICPB 3435, NBRC 102470, NCTC 9381, P. agglomerans, Pantoea herbicola, Pantoea sp. SL1_M5, Pseudomonas herbicola, bacterium G33-1
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